An aminopeptidase from bovine brain which catalyzes the hydrolysis of enkephalin.
An aminopeptidase from bovine brain which catalyzes the hydrolysis of the tyrosyl1-glycine2 bond of methionine5-enkephalin has been purified to electrophoretic homogeneity. The enzyme also catalyzes the hydrolysis of dipeptides, tripeptides, and amino acid beta-naphthylamides. The enzyme can be inactivated by dialysis against EDTA, and reconstituted with divalent metal ions. Inhibition of the enzyme is observed in the presence of p-chloromercuribenzoate and puromycin, the latter compound not being hydrolyzed by the enzyme. The enzyme is composed of a single polypeptide chain of molecular weight approx. 100,000. The properties of this enzyme are similar to those reported for other brain aminopeptidases active on enkephalin, although distinct differences are observed.
D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D001051:Apoenzymes; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D004151:Dipeptides / Q000378:metabolism; D004589:Electrophoresis, Disc; D004723:Endorphins / Q000378:metabolism*; D004745:Enkephalins / Q000378:metabolism*; D000882:Haplorhini; D008970:Molecular Weight; D011691:Puromycin / Q000494:pharmacology; D051381:Rats; D013379:Substrate Specificity
D001051:Apoenzymes; D004151:Dipeptides; D004723:Endorphins; D004745:Enkephalins; D011691:Puromycin; D000626:Aminopeptidases